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P11393

- PHEB_PORPP

UniProt

P11393 - PHEB_PORPP

Protein

B-phycoerythrin beta chain

Gene

cpeB

Organism
Porphyridium purpureum (Red alga) (Porphyridium cruentum)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    Functioni

    Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei50 – 501Phycourobilin chromophore (covalent; via 2 links)
    Binding sitei61 – 611Phycourobilin chromophore (covalent; via 2 links)
    Binding sitei82 – 821Phycoerythrobilin chromophore 1 (covalent; via 1 link)
    Binding sitei158 – 1581Phycoerythrobilin chromophore 2 (covalent; via 1 link)

    GO - Biological processi

    1. oxidation-reduction process Source: UniProtKB-KW
    2. photosynthesis Source: UniProtKB-KW
    3. protein-chromophore linkage Source: UniProtKB-KW

    Keywords - Biological processi

    Electron transport, Photosynthesis, Transport

    Keywords - Ligandi

    Bile pigment, Chromophore

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    B-phycoerythrin beta chain
    Gene namesi
    Name:cpeB
    Encoded oniPlastid; Chloroplast
    OrganismiPorphyridium purpureum (Red alga) (Porphyridium cruentum)
    Taxonomic identifieri35688 [NCBI]
    Taxonomic lineageiEukaryotaRhodophytaBangiophyceaePorphyridialesPorphyridiaceaePorphyridium

    Subcellular locationi

    Plastidchloroplast thylakoid membrane By similarity; Peripheral membrane protein By similarity; Stromal side By similarity
    Note: Forms the periphery of the phycobilisome rod.By similarity

    GO - Cellular componenti

    1. chloroplast thylakoid membrane Source: UniProtKB-SubCell
    2. phycobilisome Source: UniProtKB-KW

    Keywords - Cellular componenti

    Chloroplast, Membrane, Phycobilisome, Plastid, Thylakoid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 177177B-phycoerythrin beta chainPRO_0000199194Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei72 – 721N4-methylasparagine1 Publication

    Post-translational modificationi

    Contains two covalently linked phycoerythrobilin chromophores and one covalently linked phycourobilin chromophore.

    Keywords - PTMi

    Methylation

    Interactioni

    Subunit structurei

    Heteropolymer of 6 alpha, 6 beta and one gamma chain.By similarity

    Protein-protein interaction databases

    IntActiP11393. 1 interaction.
    MINTiMINT-8389580.

    Structurei

    Secondary structure

    1
    177
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 1411
    Helixi21 – 3212
    Helixi34 – 4512
    Helixi48 – 6215
    Helixi64 – 674
    Helixi76 – 9924
    Helixi103 – 1086
    Turni109 – 1124
    Helixi113 – 1208
    Helixi124 – 14219
    Helixi159 – 17618

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3V57X-ray1.70B/D1-177[»]
    3V58X-ray1.85B/D1-177[»]
    ProteinModelPortaliP11393.
    SMRiP11393. Positions 1-177.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the phycobiliprotein family.Curated

    Family and domain databases

    Gene3Di1.10.490.20. 1 hit.
    InterProiIPR009050. Globin-like.
    IPR012128. Phycobilisome_asu/bsu.
    [Graphical view]
    PfamiPF00502. Phycobilisome. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000081. Phycocyanin. 1 hit.
    SUPFAMiSSF46458. SSF46458. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P11393-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLDAFSRVVV NSDAKAAYVG GSDLQALKSF IADGNKRLDA VNSIVSNASC    50
    MVSDAVSGMI CENPGLISPG GNCYTNRRMA ACLRDGEIIL RYVSYALLAG 100
    DASVLEDRCL NGLKETYIAL GVPTNSSIRA VSIMKAQAVA FITNTATERK 150
    MSFAAGDCTS LASEVASYFD RVGAAIS 177
    Length:177
    Mass (Da):18,554
    Last modified:July 1, 1989 - v1
    Checksum:i168E71372A29CD89
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti167 – 1671S → Q AA sequence (PubMed:6715353)Curated

    Sequence databases

    PIRiS02818.
    RefSeqiYP_008965770.1. NC_023133.1.

    Genome annotation databases

    GeneIDi17963946.

    Cross-referencesi

    Sequence databases

    PIRi S02818.
    RefSeqi YP_008965770.1. NC_023133.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3V57 X-ray 1.70 B/D 1-177 [» ]
    3V58 X-ray 1.85 B/D 1-177 [» ]
    ProteinModelPortali P11393.
    SMRi P11393. Positions 1-177.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P11393. 1 interaction.
    MINTi MINT-8389580.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 17963946.

    Family and domain databases

    Gene3Di 1.10.490.20. 1 hit.
    InterProi IPR009050. Globin-like.
    IPR012128. Phycobilisome_asu/bsu.
    [Graphical view ]
    Pfami PF00502. Phycobilisome. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000081. Phycocyanin. 1 hit.
    SUPFAMi SSF46458. SSF46458. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The complete amino-acid sequence of the alpha and beta subunits of B-phycoerythrin from the rhodophytan alga Porphyridium cruentum."
      Sidler W., Kumpf B., Suter F., Klotz A.V., Glazer A.N., Zuber H.
      Biol. Chem. Hoppe-Seyler 370:115-124(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE, METHYLATION AT ASN-72.
    2. "Bilin attachment sites in the alpha and beta subunits of B-phycoerythrin. Amino acid sequence studies."
      Lundell D.J., Glazer A.N., DeLange R.J., Brown D.M.
      J. Biol. Chem. 259:5472-5480(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 38-77; 79-84 AND 151-171, CHROMOPHORE ATTACHMENT SITES.

    Entry informationi

    Entry nameiPHEB_PORPP
    AccessioniPrimary (citable) accession number: P11393
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 77 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3